Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Nucleosome assembly protein 1-like 1  

UniProtKB / Swiss-Prot ID :  NP1L1_HUMAN

Gene Name (Synonyms) : 
NAP1L1, NRP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. 

Protein Function :  May be involved in modulating chromatin formation and contribute to regulation of cell proliferation. 

Protein Sequence MADIDNKEQSELDQDLDDVEEVEEEETGEETKLKARQLTVQMMQNPQILAALQERLDGLVETPTGYIESL...
Predicted Secondary Structure CCCCCCCHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCHHHHHHHHHCCCCCCCCCCHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADIDN
---CCCCCC
23.59UniProtKB
Link-
10PhosphoserineNKEQSELDQ
CCHHHHHHH
41.01HPRD
Link-
10PhosphoserineNKEQSELDQ
CCHHHHHHH
41.01PhosphoELM
Link-
10PhosphoserineNKEQSELDQ
CCHHHHHHH
41.01Phosphositeplus
Link-
10PhosphoserineNKEQSELDQ
CCHHHHHHH
41.01SysPTM
Link-
10Phosphoserine.NKEQSELDQ
CCHHHHHHH
41.01UniProtKB
Link-
32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GEETKLKAR
HHHHHHHHH
51.80Phosphositeplus
Link-
39PhosphothreonineARQLTVQMM
HHHHHHHHH
10.60Phosphositeplus
Link-
57Caspase cleavage aspartic acidQERLDGLVE
HHCCCCCCC
55.38Phosphositeplus
Link-
62PhosphothreonineGLVETPTGY
CCCCCCCHH
20.76HPRD
Link-
62PhosphothreonineGLVETPTGY
CCCCCCCHH
20.76PhosphoELM
Link-
62PhosphothreonineGLVETPTGY
CCCCCCCHH
20.76Phosphositeplus
Link-
62PhosphothreonineGLVETPTGY
CCCCCCCHH
20.76SysPTM
Link-
62Phosphothreonine.GLVETPTGY
CCCCCCCHH
20.76UniProtKB
Link-
64PhosphothreonineVETPTGYIE
CCCCCHHHH
50.46HPRD
Link-
64PhosphothreonineVETPTGYIE
CCCCCHHHH
50.46PhosphoELM
Link-
64PhosphothreonineVETPTGYIE
CCCCCHHHH
50.46Phosphositeplus
Link-
64PhosphothreonineVETPTGYIE
CCCCCHHHH
50.46SysPTM
Link-
66PhosphotyrosineTPTGYIESL
CCCHHHHHH
12.18HPRD
Link-
66PhosphotyrosineTPTGYIESL
CCCHHHHHH
12.18PhosphoELM
Link-
66PhosphotyrosineTPTGYIESL
CCCHHHHHH
12.18Phosphositeplus
Link-
69PhosphoserineGYIESLPRV
HHHHHHHHH
33.83HPRD
Link-
69PhosphoserineGYIESLPRV
HHHHHHHHH
33.83PhosphoELM
Link-
69PhosphoserineGYIESLPRV
HHHHHHHHH
33.83Phosphositeplus
Link-
69PhosphoserineGYIESLPRV
HHHHHHHHH
33.83SysPTM
Link-
69Phosphoserine.GYIESLPRV
HHHHHHHHH
33.83UniProtKB
Link-
82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VNALKNLQV
HHHHHHHHH
53.88Phosphositeplus
Link-
105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DLERKYAVL
HHHHHHHHH
28.34Phosphositeplus
Link-
116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PLFDKRFEI
HHHHHHHHH
52.21Phosphositeplus
Link-
116N6-acetyllysinePLFDKRFEI
HHHHHHHHH
52.21HPRD
Link-
116N6-acetyllysinePLFDKRFEI
HHHHHHHHH
52.21Phosphositeplus
Link-
116N6-acetyllysine.PLFDKRFEI
HHHHHHHHH
52.21UniProtKB
Link-
143PhosphoserineEDEISEELK
HHHHHHHHH
23.99HPRD
Link-
143PhosphoserineEDEISEELK
HHHHHHHHH
23.99PhosphoELM
Link-
143PhosphoserineEDEISEELK
HHHHHHHHH
23.99Phosphositeplus
Link-
143PhosphoserineEDEISEELK
HHHHHHHHH
23.99SysPTM
Link-
143Phosphoserine.EDEISEELK
HHHHHHHHH
23.99UniProtKB
Link-
165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KEDPKGIPE
CCCCCCCCH
80.11Phosphositeplus
Link-
165N6-acetyllysineKEDPKGIPE
CCCCCCCCH
80.11Phosphositeplus
Link-
194N6-acetyllysineEPILKHLKD
HHHHHHHCC
47.84HPRD
Link-
381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YDPKKDQNP
CCCCCCCCC
70.68Phosphositeplus
Link-
388S-farnesyl cysteineNPAECKQQ
CCHHHCCC
5.39HPRD
Link-
388S-farnesyl cysteine.NPAECKQQ
CCHHHCCC
5.39UniProtKB
Link-
389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PAECKQQ
CHHHCCC
43.15Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TNR1A_HUMANphysical interactionMINT-49327MINT14743216
PSMD4_HUMANphysical interactionMINT-3372988MINT16990800
NP1L1_HUMANphysical interactionMINT-63872MINT16169070
TRADD_HUMANphysical interactionMINT-49479MINT14743216
Q53F97_HUMANphysical interactionMINT-63873MINT16169070
Q86TQ8_HUMANphysical interactionMINT-63874MINT16169070
TANK_HUMANphysical interactionMINT-48257MINT14743216
NP1L1_HUMANphysical interactionEBI-735196
intact16169070
ODO2_HUMANphysical interactionEBI-732590
intact16169070
FSD1_HUMANphysical interactionEBI-737219
intact16169070
Q9BTV5_HUMANphysical interactionEBI-737219
intact16169070
HBA_HUMANphysical interactionEBI-737222
intact16169070
1B42_HUMANphysical interactionEBI-1083140
intact17353931
CBP_HUMANin vitroHPRD:01248HPRD11940655
EP300_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01248HPRD11940655
NP1L1_HUMANyeast 2-hybridHPRD:01248HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-62, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND THR-62, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-62; SER-69 ANDSER-143, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-62, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-69, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASSSPECTROMETRY.
Prenylation
ReferencePubMed
"A tagging-via-substrate technology for detection and proteomics offarnesylated proteins.";
Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J.,Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.;
Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004).
Cited for: ISOPRENYLATION AT CYS-388.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures